Investigating the Role of JIP3's JNK Binding Domain in Glutamate Receptor Transport
Category: Research Poster
Author(s): Alex Kowal, Ariel Michaelis
Presenter(s): Alex Kowal
Mentors(s): Frederic Hoerndli
C. Elegans is a great model organism for studying trafficking of proteins in the neuron due to the ease of visualizing one pair of neurons called the AVA. Since the worm is transparent, we can see specific transport dynamics by attaching a fluorescent marker to the proteins being transported. In our study we will test how mutating the JNK binding domain of JIP3 (UNC-16 in C. Elegans), which is an adapter protein responsible for binding vesicles to a kinesin motor, affects transport dynamics in the AVA neurons. Previous work has shown that mutations in JNK signaling lead to delocalization of vesicular cargo, and we hope to demonstrate how deleting the JNK binding domain affects transport dynamics of glutamate receptors. To accomplish this, we will first create an unmutated UNC-16 and a UNC-16 with a deleted JNK binding domain strain, both tagged with a red fluorescent marker called mCherry. We will then cross those strains with a GFP tagged GLR1 receptor to visualize how the transport of GLR1 is affected when compared to a baseline GFP/GLR1 worm. We will use confocal microscopy to visualize how these transport events are affected. While no data has been collected to date, we expect glutamate receptor transport events to decrease in the mutated UNC-16 strain while the unmutated strain is expected to remain relatively consistent with our akis-141 wild type controls.